CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008571
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Biliverdin reductase A 
Protein Synonyms/Alias
 BVR A; Biliverdin-IX alpha-reductase 
Gene Name
 BLVRA 
Gene Synonyms/Alias
 BLVR; BVR 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
219PLSWIEEKGPGLKRNubiquitination[1, 2]
234RYLSFHFKSGSLENVubiquitination[1, 2]
248VPNVGVNKNIFLKDQacetylation[3, 4]
248VPNVGVNKNIFLKDQubiquitination[1, 2, 5, 6]
253VNKNIFLKDQNIFVQacetylation[3]
253VNKNIFLKDQNIFVQubiquitination[1, 2]
261DQNIFVQKLLGQFSEubiquitination[1, 2, 7, 8]
269LLGQFSEKELAAEKKacetylation[4, 6, 9, 10, 11]
269LLGQFSEKELAAEKKubiquitination[1, 2, 5, 6, 8]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [10] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [11] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
 Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor. 
Sequence Annotation
 NP_BIND 15 20 NAD or NADP.
 NP_BIND 44 46 NAD or NADP.
 NP_BIND 77 80 NAD or NADP.
 METAL 280 280 Zinc (Potential).
 METAL 281 281 Zinc (Potential).
 METAL 292 292 Zinc (Potential).
 METAL 293 293 Zinc (Potential).
 BINDING 98 98 NAD or NADP; via carbonyl oxygen.
 MOD_RES 174 174 Phosphothreonine.
 MOD_RES 178 178 Phosphoserine.
 MOD_RES 230 230 Phosphoserine.
 MOD_RES 248 248 N6-acetyllysine.
 MOD_RES 253 253 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; NADP; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 296 AA 
Protein Sequence
MNAEPERKFG VVVVGVGRAG SVRMRDLRNP HPSSAFLNLI GFVSRRELGS IDGVQQISLE 60
DALSSQEVEV AYICSESSSH EDYIRQFLNA GKHVLVEYPM TLSLAAAQEL WELAEQKGKV 120
LHEEHVELLM EEFAFLKKEV VGKDLLKGSL LFTAGPLEEE RFGFPAFSGI SRLTWLVSLF 180
GELSLVSATL EERKEDQYMK MTVCLETEKK SPLSWIEEKG PGLKRNRYLS FHFKSGSLEN 240
VPNVGVNKNI FLKDQNIFVQ KLLGQFSEKE LAAEKKRILH CLGLAEEIQK YCCSRK 296 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0004074; F:biliverdin reductase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0042167; P:heme catabolic process; TAS:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR017094; Biliverdin_Rdtase_A.
 IPR015249; Biliverdin_Rdtase_cat.
 IPR016040; NAD(P)-bd_dom.
 IPR000683; Oxidoreductase_N. 
Pfam
 PF09166; Biliv-reduc_cat
 PF01408; GFO_IDH_MocA 
SMART
  
PROSITE
  
PRINTS